CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003345
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Bifunctional protein GlmU 
Protein Synonyms/Alias
 UDP-N-acetylglucosamine pyrophosphorylase; N-acetylglucosamine-1-phosphate uridyltransferase; Glucosamine-1-phosphate N-acetyltransferase 
Gene Name
 glmU 
Gene Synonyms/Alias
 yieA; b3730; JW3708 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
25RMYSDLPKVLHTLAGacetylation[1]
63GHGGDLLKQALKDDNacetylation[1]
132GIGLLTVKLDDPTGYacetylation[1]
156VTGIVEHKDATDEQRacetylation[1]
246YQSEQAEKLLLAGVMacetylation[1]
351VGNFVEMKKARLGKGacetylation[1, 2]
360ARLGKGSKAGHLTYLacetylation[1]
392CNYDGANKFKTIIGDacetylation[1]
Reference
 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618]
 [2] Comprehensive profiling of protein lysine acetylation in Escherichia coli.
 Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z.
 J Proteome Res. 2013 Feb 1;12(2):844-51. [PMID: 23294111
Functional Description
 Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP- GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5- monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain. 
Sequence Annotation
 REGION 1 229 Pyrophosphorylase.
 REGION 11 14 UDP-GlcNAc binding.
 REGION 81 82 UDP-GlcNAc binding.
 REGION 103 105 UDP-GlcNAc binding.
 REGION 230 250 Linker.
 REGION 251 456 N-acetyltransferase.
 REGION 386 387 Acetyl-CoA binding.
 ACT_SITE 363 363 Proton acceptor (By similarity).
 METAL 105 105 Magnesium.
 METAL 227 227 Magnesium.
 BINDING 25 25 UDP-GlcNAc (By similarity).
 BINDING 76 76 UDP-GlcNAc.
 BINDING 140 140 UDP-GlcNAc; via amide nitrogen.
 BINDING 154 154 UDP-GlcNAc.
 BINDING 169 169 UDP-GlcNAc.
 BINDING 227 227 UDP-GlcNAc (By similarity).
 BINDING 333 333 UDP-GlcNAc.
 BINDING 351 351 UDP-GlcNAc.
 BINDING 366 366 UDP-GlcNAc.
 BINDING 377 377 UDP-GlcNAc.
 BINDING 380 380 Acetyl-CoA; via amide nitrogen.
 BINDING 405 405 Acetyl-CoA.
 BINDING 423 423 Acetyl-CoA; via amide nitrogen.
 BINDING 440 440 Acetyl-CoA.  
Keyword
 3D-structure; Acyltransferase; Cell shape; Cell wall biogenesis/degradation; Cobalt; Complete proteome; Cytoplasm; Magnesium; Metal-binding; Multifunctional enzyme; Nucleotidyltransferase; Peptidoglycan synthesis; Reference proteome; Repeat; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 456 AA 
Protein Sequence
MLNNAMSVVI LAAGKGTRMY SDLPKVLHTL AGKAMVQHVI DAANELGAAH VHLVYGHGGD 60
LLKQALKDDN LNWVLQAEQL GTGHAMQQAA PFFADDEDIL MLYGDVPLIS VETLQRLRDA 120
KPQGGIGLLT VKLDDPTGYG RITRENGKVT GIVEHKDATD EQRQIQEINT GILIANGADM 180
KRWLAKLTNN NAQGEYYITD IIALAYQEGR EIVAVHPQRL SEVEGVNNRL QLSRLERVYQ 240
SEQAEKLLLA GVMLRDPARF DLRGTLTHGR DVEIDTNVII EGNVTLGHRV KIGTGCVIKN 300
SVIGDDCEIS PYTVVEDANL AAACTIGPFA RLRPGAELLE GAHVGNFVEM KKARLGKGSK 360
AGHLTYLGDA EIGDNVNIGA GTITCNYDGA NKFKTIIGDD VFVGSDTQLV APVTVGKGAT 420
IAAGTTVTRN VGENALAISR VPQTQKEGWR RPVKKK 456 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0019134; F:glucosamine-1-phosphate N-acetyltransferase activity; IDA:EcoCyc.
 GO:0042802; F:identical protein binding; IDA:EcoCyc.
 GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
 GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; IDA:EcoCyc.
 GO:0000902; P:cell morphogenesis; IEA:HAMAP.
 GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniPathway.
 GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:InterPro.
 GO:0009252; P:peptidoglycan biosynthetic process; IEA:HAMAP.
 GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
 GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IMP:EcoCyc. 
Interpro
 IPR005882; Bifunctional_GlmU.
 IPR001451; Hexapep_transf.
 IPR018357; Hexapep_transf_CS.
 IPR025877; MobA-like_NTP_Trfase_dom.
 IPR011004; Trimer_LpxA-like. 
Pfam
 PF00132; Hexapep
 PF12804; NTP_transf_3 
SMART
  
PROSITE
 PS00101; HEXAPEP_TRANSFERASES 
PRINTS